Intrinsically disordered proteins lack a hydrophobic core, and have high densities of charged amino acid residues such as Lys, Arg, and Glu. Pro residues are also prominent, as they tend to disrupt ordered structures.

TLS Online TPP Program

#Id: 8760

#Unit 1. Molecules and their Interaction Relevant to Biology

This is because hydrogen-bonding groups in an unfolded protein form hydrogen bonds with water molecules. Thus the contribution of a hydrogen bond to the stability of a native protein is the small difference in hydrogen bonding free energies between the native and unfolded states (−2 to 8 kJ ∙ mol−1)

TLS Online TPP Program

#Id: 2839

#Unit 13. Methods in Biology

These histidine's are separated by using Nickel-chelate-nitrilotriacetate (Ni-NTA) chromatography column.

TLS Online TPP Program

#Id: 5533

#Unit 7. System Physiology – Animal

Descending part of the thin segment is highly permeable to water and moderately permeable to most Solutes (urea and sodium)

TLS Online TPP Program

#Id: 612

#Unit 2. Cellular Organization

Repression-Trp aporepressor dimer binds high tryptophan, changes conformation with high affinity for trp operator Tryptophan is a corepressor

 

TLS Online TPP Program

#Id: 7798

#Unit 2. Cellular Organization

Exportin-t

functions to export tRNAs & binds fully processed tRNAs in a complex with Ran⋅GTP